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Novel regulation of PLCζ activity via its XY-linker
Michail Nomikos1, Khalil Elgmati, Maria Theodoridou
1Department of Obstetrics and Gynaecology, Cardiff University School of Medicine, Cardiff CF14 4XN, UK. mixosn@yahoo.com
Abstract:
The XY-linker region of somatic cell PLC (phospholipase)-β, -γ, -δ and -ε isoforms confers potent catalytic inhibition, suggesting a common auto-regulatory role. Surprisingly, the sperm PLCζ XY-linker does not mediate auto-inhibition. Unlike for somatic PLCs, the absence of the PLCζ XY-linker significantly diminishes both in vitro PIP2 (phosphatidylinositol 4,5-bisphosphate) hydrolysis and in vivo Ca2+-oscillation-inducing activity, revealing evidence for a novel PLCζ enzymatic mechanism.
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